Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea

Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are...

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Bibliographic Details
Published in:PLoS biology 2021-06, Vol.19 (6), p.e3001277-e3001277
Main Authors: Schulze, Stefan, Pfeiffer, Friedhelm, Garcia, Benjamin A, Pohlschroder, Mechthild
Format: Article
Language:English
Subjects:
Acids
Archaea
Archaeabacteria
Biofilms
Biology and Life Sciences
Biosynthesis
Cell culture
Complexity
Datasets
Enzymes
Eukaryotes
Glycopeptides
Glycoproteins
Glycosylation
Methods and Resources
Microbiological research
Morphology
Motility
Mutants
Physiological aspects
Prokaryotes
Proteins
Proteomes
Proteomics
Research and Analysis Methods
Spectrometry
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Summary:Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.
ISSN:1545-7885
1544-9173
1545-7885
DOI:10.1371/journal.pbio.3001277